Magnesium in PDB 5zwo: Cryo-Em Structure of the Yeast B Complex at Average Resolution of 3.9 Angstrom

All present enzymatic activity of Cryo-Em Structure of the Yeast B Complex at Average Resolution of 3.9 Angstrom:
3.6.4.13;

The binding sites of Magnesium atom in the Cryo-Em Structure of the Yeast B Complex at Average Resolution of 3.9 Angstrom (pdb code 5zwo). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Cryo-Em Structure of the Yeast B Complex at Average Resolution of 3.9 Angstrom, PDB code: 5zwo:

Magnesium binding site 1 out of 1 in the Cryo-Em Structure of the Yeast B Complex at Average Resolution of 3.9 Angstrom


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryo-Em Structure of the Yeast B Complex at Average Resolution of 3.9 Angstrom within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg1501 b:30.7 occ:1.00 OG1 C:THR147 1.5 32.4 1.0 O1G C:GTP1500 1.9 19.3 1.0 OG C:SER190 2.1 55.6 1.0 O2B C:GTP1500 2.3 21.9 1.0 CB C:THR147 2.6 37.6 1.0 O3A C:GTP1500 2.9 32.3 1.0 N C:THR147 3.0 36.8 1.0 PB C:GTP1500 3.1 21.4 1.0 PG C:GTP1500 3.2 17.9 1.0 CB C:SER190 3.3 53.9 1.0 CA C:THR147 3.3 34.5 1.0 O3G C:GTP1500 3.6 19.0 1.0 O3B C:GTP1500 3.8 22.1 1.0 CG2 C:THR147 3.8 49.5 1.0 CB C:LYS146 3.8 42.4 1.0 C C:LYS146 4.1 41.5 1.0 CE C:LYS146 4.1 55.7 1.0 O C:ALA215 4.2 33.6 1.0 PA C:GTP1500 4.2 48.9 1.0 OD1 C:ASP214 4.3 0.9 1.0 O2G C:GTP1500 4.4 20.6 1.0 OD2 C:ASP214 4.4 0.1 1.0 O1A C:GTP1500 4.4 41.5 1.0 O1B C:GTP1500 4.4 23.2 1.0 N C:SER190 4.4 38.4 1.0 CA C:LYS146 4.4 39.9 1.0 CA C:SER190 4.5 42.3 1.0 N C:LYS146 4.7 37.6 1.0 NZ C:LYS146 4.7 58.9 1.0 CG C:ASP214 4.7 0.4 1.0 C C:THR147 4.7 33.7 1.0 O2A C:GTP1500 4.8 62.1 1.0 CG C:LYS146 4.9 45.9 1.0 CD C:LYS146 5.0 49.2 1.0

R.Bai, R.Wan, C.Yan, J.Lei, Y.Shi. Structures of the Fully Assembledsaccharomyces Cerevisiaespliceosome Before Activation Science V. 360 1423 2018.
ISSN: ESSN 1095-9203
PubMed: 29794219
DOI: 10.1126/SCIENCE.AAU0325